Pub. Date : 2009 May 12
PMID : 19435523
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Chibby forms a homodimer through a heptad repeat of leucine residues in its C-terminal coiled-coil motif. | Leucine | chibby family member 1, beta catenin antagonist | Homo sapiens |
2 | Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction. | Alanine | chibby family member 1, beta catenin antagonist | Homo sapiens |
3 | Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction. | Alanine | chibby family member 1, beta catenin antagonist | Homo sapiens |
4 | Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction. | Leucine | chibby family member 1, beta catenin antagonist | Homo sapiens |
5 | Alanine substitutions of two or more of four critical leucine residues within the C-terminal heptad repeats completely eliminate the Cby-Cby interaction. | Leucine | chibby family member 1, beta catenin antagonist | Homo sapiens |
6 | CONCLUSION: Our comprehensive mutational analysis of the Cby coiled-coil domain reveals that the four heptad leucine residues play an essential role in mediating Cby homodimerization. | Leucine | chibby family member 1, beta catenin antagonist | Homo sapiens |
7 | CONCLUSION: Our comprehensive mutational analysis of the Cby coiled-coil domain reveals that the four heptad leucine residues play an essential role in mediating Cby homodimerization. | Leucine | chibby family member 1, beta catenin antagonist | Homo sapiens |